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P25398

- RS12_HUMAN

UniProt

P25398 - RS12_HUMAN

Protein

40S ribosomal protein S12

Gene

RPS12

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. structural constituent of ribosome Source: InterPro

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. gene expression Source: Reactome
    3. mRNA metabolic process Source: Reactome
    4. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
    5. RNA metabolic process Source: Reactome
    6. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
    7. translation Source: UniProtKB
    8. translational elongation Source: Reactome
    9. translational initiation Source: Reactome
    10. translational termination Source: Reactome
    11. viral life cycle Source: Reactome
    12. viral process Source: Reactome
    13. viral transcription Source: Reactome

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Enzyme and pathway databases

    ReactomeiREACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
    REACT_115902. SRP-dependent cotranslational protein targeting to membrane.
    REACT_1404. Peptide chain elongation.
    REACT_1797. Formation of a pool of free 40S subunits.
    REACT_1979. Translation initiation complex formation.
    REACT_1986. Eukaryotic Translation Termination.
    REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
    REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
    REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
    REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
    REACT_931. Ribosomal scanning and start codon recognition.
    REACT_9491. Viral mRNA Translation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    40S ribosomal protein S12
    Gene namesi
    Name:RPS12
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:10385. RPS12.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. cytosolic small ribosomal subunit Source: UniProtKB
    3. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34784.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed5 Publications
    Chaini2 – 13213140S ribosomal protein S12PRO_0000122323Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine5 Publications
    Modified residuei129 – 1291N6-succinyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP25398.
    PaxDbiP25398.
    PRIDEiP25398.

    2D gel databases

    UCD-2DPAGEP25398.

    PTM databases

    PhosphoSiteiP25398.

    Expressioni

    Gene expression databases

    BgeeiP25398.
    CleanExiHS_RPS12.
    GenevestigatoriP25398.

    Organism-specific databases

    HPAiHPA006124.

    Interactioni

    Protein-protein interaction databases

    BioGridi112120. 95 interactions.
    IntActiP25398. 12 interactions.
    MINTiMINT-1160578.
    STRINGi9606.ENSP00000230050.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3J3Aelectron microscopy5.00M1-132[»]
    ProteinModelPortaliP25398.
    SMRiP25398. Positions 9-132.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein S12e family.Curated

    Phylogenomic databases

    eggNOGiCOG1358.
    HOGENOMiHOG000210688.
    HOVERGENiHBG001720.
    InParanoidiP25398.
    KOiK02951.
    OMAiANNCDEP.
    OrthoDBiEOG7H1JP3.
    PhylomeDBiP25398.
    TreeFamiTF300196.

    Family and domain databases

    Gene3Di3.30.1330.30. 1 hit.
    InterProiIPR029064. L30e-like.
    IPR004038. Ribosomal_L7Ae/L30e/S12e/Gad45.
    IPR000530. Ribosomal_S12e.
    [Graphical view]
    PANTHERiPTHR11843. PTHR11843. 1 hit.
    PfamiPF01248. Ribosomal_L7Ae. 1 hit.
    [Graphical view]
    PRINTSiPR00972. RIBSOMALS12E.
    SUPFAMiSSF55315. SSF55315. 1 hit.
    PROSITEiPS01189. RIBOSOMAL_S12E. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P25398-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAEEGIAAGG VMDVNTALQE VLKTALIHDG LARGIREAAK ALDKRQAHLC    50
    VLASNCDEPM YVKLVEALCA EHQINLIKVD DNKKLGEWVG LCKIDREGKP 100
    RKVVGCSCVV VKDYGKESQA KDVIEEYFKC KK 132
    Length:132
    Mass (Da):14,515
    Last modified:March 3, 2009 - v3
    Checksum:i45AD1274D55FFA25
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti52 – 521L → Q in CAA37582. (PubMed:1861993)Curated
    Sequence conflicti69 – 691C → L in CAA37582. (PubMed:1861993)Curated
    Sequence conflicti99 – 991K → N in CAA37582. (PubMed:1861993)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53505 mRNA. Translation: CAA37582.1.
    AB061840 Genomic DNA. Translation: BAB79478.1.
    AK311826 mRNA. Translation: BAG34768.1.
    AL137783 Genomic DNA. Translation: CAC12946.1.
    CH471051 Genomic DNA. Translation: EAW48011.1.
    BC017321 mRNA. Translation: AAH17321.1.
    BC071930 mRNA. Translation: AAH71930.1.
    BC095424 mRNA. Translation: AAH95424.1.
    AB007153 Genomic DNA. Translation: BAA25819.1.
    CCDSiCCDS5164.1.
    PIRiS22989. R3HU12.
    RefSeqiNP_001007.2. NM_001016.3.
    UniGeneiHs.546289.

    Genome annotation databases

    EnsembliENST00000230050; ENSP00000230050; ENSG00000112306.
    GeneIDi6206.
    KEGGihsa:6206.
    UCSCiuc003qdx.3. human.

    Polymorphism databases

    DMDMi224471878.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53505 mRNA. Translation: CAA37582.1 .
    AB061840 Genomic DNA. Translation: BAB79478.1 .
    AK311826 mRNA. Translation: BAG34768.1 .
    AL137783 Genomic DNA. Translation: CAC12946.1 .
    CH471051 Genomic DNA. Translation: EAW48011.1 .
    BC017321 mRNA. Translation: AAH17321.1 .
    BC071930 mRNA. Translation: AAH71930.1 .
    BC095424 mRNA. Translation: AAH95424.1 .
    AB007153 Genomic DNA. Translation: BAA25819.1 .
    CCDSi CCDS5164.1.
    PIRi S22989. R3HU12.
    RefSeqi NP_001007.2. NM_001016.3.
    UniGenei Hs.546289.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3J3A electron microscopy 5.00 M 1-132 [» ]
    ProteinModelPortali P25398.
    SMRi P25398. Positions 9-132.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112120. 95 interactions.
    IntActi P25398. 12 interactions.
    MINTi MINT-1160578.
    STRINGi 9606.ENSP00000230050.

    PTM databases

    PhosphoSitei P25398.

    Polymorphism databases

    DMDMi 224471878.

    2D gel databases

    UCD-2DPAGE P25398.

    Proteomic databases

    MaxQBi P25398.
    PaxDbi P25398.
    PRIDEi P25398.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000230050 ; ENSP00000230050 ; ENSG00000112306 .
    GeneIDi 6206.
    KEGGi hsa:6206.
    UCSCi uc003qdx.3. human.

    Organism-specific databases

    CTDi 6206.
    GeneCardsi GC06P133136.
    HGNCi HGNC:10385. RPS12.
    HPAi HPA006124.
    MIMi 603660. gene.
    neXtProti NX_P25398.
    PharmGKBi PA34784.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1358.
    HOGENOMi HOG000210688.
    HOVERGENi HBG001720.
    InParanoidi P25398.
    KOi K02951.
    OMAi ANNCDEP.
    OrthoDBi EOG7H1JP3.
    PhylomeDBi P25398.
    TreeFami TF300196.

    Enzyme and pathway databases

    Reactomei REACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
    REACT_115902. SRP-dependent cotranslational protein targeting to membrane.
    REACT_1404. Peptide chain elongation.
    REACT_1797. Formation of a pool of free 40S subunits.
    REACT_1979. Translation initiation complex formation.
    REACT_1986. Eukaryotic Translation Termination.
    REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
    REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
    REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
    REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
    REACT_931. Ribosomal scanning and start codon recognition.
    REACT_9491. Viral mRNA Translation.

    Miscellaneous databases

    ChiTaRSi RpS12. human.
    GeneWikii RPS12.
    GenomeRNAii 6206.
    NextBioi 24103.
    PROi P25398.
    SOURCEi Search...

    Gene expression databases

    Bgeei P25398.
    CleanExi HS_RPS12.
    Genevestigatori P25398.

    Family and domain databases

    Gene3Di 3.30.1330.30. 1 hit.
    InterProi IPR029064. L30e-like.
    IPR004038. Ribosomal_L7Ae/L30e/S12e/Gad45.
    IPR000530. Ribosomal_S12e.
    [Graphical view ]
    PANTHERi PTHR11843. PTHR11843. 1 hit.
    Pfami PF01248. Ribosomal_L7Ae. 1 hit.
    [Graphical view ]
    PRINTSi PR00972. RIBSOMALS12E.
    SUPFAMi SSF55315. SSF55315. 1 hit.
    PROSITEi PS01189. RIBOSOMAL_S12E. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA and predicted amino acid sequences of the human ribosomal protein genes rpS12 and rpL17."
      Herault Y., Michel D., Chatelain G., Brun G.
      Nucleic Acids Res. 19:4001-4001(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The human ribosomal protein genes: sequencing and comparative analysis of 73 genes."
      Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S., Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.
      Genome Res. 12:379-390(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Testis.
    4. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Embryonic stem cell and Skin.
    7. Cited for: PROTEIN SEQUENCE OF 2-33; 85-93 AND 117-129, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Cervix carcinoma, Hepatoma and Mammary carcinoma.
    8. "Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry."
      Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K., Egorov T.A., Thiede B., Wittmann-Liebold B., Otto A.
      Eur. J. Biochem. 239:144-149(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 24-39.
      Tissue: Placenta.
    9. "A map of 75 human ribosomal protein genes."
      Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., Hudson T.J., Tanaka T., Page D.C.
      Genome Res. 8:509-523(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 113-125.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

    Entry informationi

    Entry nameiRS12_HUMAN
    AccessioniPrimary (citable) accession number: P25398
    Secondary accession number(s): Q76M58
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: March 3, 2009
    Last modified: October 1, 2014
    This is version 136 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. Ribosomal proteins
      Ribosomal proteins families and list of entries
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3